ID PUR5_DINSH Reviewed; 353 AA. AC A8LNB8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741}; DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741}; GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741}; GN OrderedLocusNames=Dshi_1889; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12; RX PubMed=19741735; DOI=10.1038/ismej.2009.94; RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I., RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C., RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W., RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T., RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S., RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A., RA Zech H., Simon M.; RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae: RT a hitchhiker's guide to life in the sea."; RL ISME J. 4:61-77(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00741}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_00741}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}. CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000255|HAMAP- CC Rule:MF_00741}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000830; ABV93631.1; -; Genomic_DNA. DR RefSeq; WP_012178561.1; NC_009952.1. DR AlphaFoldDB; A8LNB8; -. DR SMR; A8LNB8; -. DR STRING; 398580.Dshi_1889; -. DR KEGG; dsh:Dshi_1889; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_5; -. DR OrthoDB; 9777881at2; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000006833; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02196; PurM; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_00741; AIRS; 1. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR004733; PurM_cligase. DR NCBIfam; TIGR00878; purM; 1. DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1. DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1..353 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000083457" SQ SEQUENCE 353 AA; 35828 MW; C4011C68C0728E88 CRC64; MTTDTPPPKP GLTYAEAGVD IDAGNTLVDR IKPAAKATSR PGVMSGLGGF GALFDLRAAG YADPVLVAAT DGVGTKLRIA IDTGHVDTIG IDLVAMCVND LVCQGAEPLL FLDYFATGKL DVAEAATIVE GIARGCATSG CALIGGETAE MPGMYAKGDF DLAGFAVGAM ERGGALPANV AAGDMILGLA SDGVHSNGYS LVRRIVERSG LGWGDPAPFE GRTLGAALLT PTRLYVQPAL AAIRAGGVHG LAHVTGGGLT ENLPRVLPEG LGIEINLGAW ELPPVFRWLA AEGGLDEAEL LKTFNAGIGM ALIVAPDRAE ALADLLAGAG ERVAVIGHVT EGAGAVHYRG TLL //